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Protein

Synaptotagmin-like protein 3

Gene

Sytl3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May act as Rab effector protein and play a role in vesicle trafficking. Binds phospholipids in the presence of calcium ions.

GO - Molecular functioni

  • calcium-dependent phospholipid binding Source: UniProtKB
  • calcium ion binding Source: GO_Central
  • clathrin binding Source: GO_Central
  • neurexin family protein binding Source: UniProtKB
  • phospholipid binding Source: MGI
  • syntaxin binding Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptotagmin-like protein 3
Alternative name(s):
Exophilin-6
Gene namesi
Name:Sytl3
Synonyms:Slp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1933367. Sytl3.

Subcellular locationi

GO - Cellular componenti

  • exocytic vesicle Source: GO_Central
  • extrinsic component of plasma membrane Source: UniProtKB
  • membrane Source: MGI
  • plasma membrane Source: GO_Central
  • presynapse Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi336 – 3372EE → QQ: Binds phospholipids only in the absence of divalent cations. 1 Publication
Mutagenesisi359 – 3613KRK → QQQ: Binds phospholipids only in the absence of divalent cations. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607Synaptotagmin-like protein 3PRO_0000190215Add
BLAST

Proteomic databases

EPDiQ99N48.
PaxDbiQ99N48.
PRIDEiQ99N48.

PTM databases

iPTMnetiQ99N48.
PhosphoSiteiQ99N48.

Expressioni

Tissue specificityi

Highly expressed in spleen and lung. Detected at lower levels in heart and testis.1 Publication

Gene expression databases

BgeeiQ99N48.
CleanExiMM_SYTL3.
ExpressionAtlasiQ99N48. baseline and differential.
GenevisibleiQ99N48. MM.

Interactioni

Subunit structurei

Monomer. Binds NRXN1. Binds RAB27A that has been activated by GTP-binding via its N-terminus.

GO - Molecular functioni

  • clathrin binding Source: GO_Central
  • neurexin family protein binding Source: UniProtKB
  • syntaxin binding Source: GO_Central

Protein-protein interaction databases

IntActiQ99N48. 2 interactions.
STRINGi10090.ENSMUSP00000095041.

Structurei

3D structure databases

ProteinModelPortaliQ99N48.
SMRiQ99N48. Positions 8-122, 266-596.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 123120RabBDPROSITE-ProRule annotationAdd
BLAST
Domaini307 – 411105C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini464 – 568105C2 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 RabBD (Rab-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00810000125376.
HOVERGENiHBG103087.
InParanoidiQ99N48.
KOiK17598.
OMAiFVKGCLT.
OrthoDBiEOG7P02HG.
PhylomeDBiQ99N48.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR010911. Rab_BD.
IPR028704. SYTL3.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10024:SF222. PTHR10024:SF222. 1 hit.
PfamiPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99N48-1) [UniParc]FASTAAdd to basket

Also known as: Slp3-a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAHEVDLESF KELERDIILR VLYRDQTVQS TEEERVRKLK SHLQHLRWKG
60 70 80 90 100
AKSSSQEYKE KCCARCQRAL GLLLNRGAVC QGCSHRVCSE CRVFLRRTRA
110 120 130 140 150
WKCTVCFEDR NVKIKTGEWF FEERARKFPT AGRRETAGAK LLQSYQRLSK
160 170 180 190 200
ISVVPPTPPP FSESQCSSSS RLQELGHFRG FNKSVENLFL SVTTQMRKLS
210 220 230 240 250
KSQNDMTSEK HLLAMDPRQC VGHTERRSQS DTAVNVTSRK ASTPDILKAF
260 270 280 290 300
HQEDPKHPPD PVLKQDTPPS SPTHSAVFSG GLRHGSLISI NSTCTEMGNF
310 320 330 340 350
DNANVTGEIE FAIHYCVKSC SLEICIKTCK NLAYGEEKKR KCNPYVKTYL
360 370 380 390 400
LPDRSSQGKR KTRVQKNTLD PTFEETLKYQ VDPGQLMTRR LQVSVWHLGT
410 420 430 440 450
LARRVFLGEV ILPLAMWDFK DSTAQNARWY PLRAKAEKYE ENIPQNNGEL
460 470 480 490 500
AVRAKLVLPA GPRKPQEAQE GQLALNGQLC LVVLGAKNLP VRSDGTLNSF
510 520 530 540 550
VKGCLTLPNQ QKLRVKSPVL KKQACPQWKH SFVFNGVSSS QLRQSTLELT
560 570 580 590 600
VWDQAIFGMN DRLLGEARLG SKGGAAGCPD SGSQSKLQWH RVLSSPNLWT

DMTLVLH
Length:607
Mass (Da):68,568
Last modified:July 25, 2003 - v2
Checksum:iF9F404D2D77A6351
GO
Isoform 2 (identifier: Q99N48-2) [UniParc]FASTAAdd to basket

Also known as: Slp3-a + 3S-I

The sequence of this isoform differs from the canonical sequence as follows:
     1-195: Missing.

Show »
Length:412
Mass (Da):45,955
Checksum:iAB1EDD538CCCB218
GO
Isoform 3 (identifier: Q99N48-3) [UniParc]FASTAAdd to basket

Also known as: Slp3-b, Slp3-a delta 3S-II

The sequence of this isoform differs from the canonical sequence as follows:
     1-214: Missing.

Show »
Length:393
Mass (Da):43,755
Checksum:iD6D27768F455F91B
GO
Isoform 4 (identifier: Q99N48-4) [UniParc]FASTAAdd to basket

Also known as: Slp3-b + 3S-III

The sequence of this isoform differs from the canonical sequence as follows:
     1-296: Missing.

Show »
Length:311
Mass (Da):34,884
Checksum:i91986B928DC510E0
GO
Isoform 5 (identifier: Q99N48-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     111-114: NVKI → ANGR
     115-607: Missing.

Note: No experimental confirmation available.
Show »
Length:114
Mass (Da):13,429
Checksum:i5EBD2E5BBFDAE4C6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti229 – 2291Q → R in BAB32653 (PubMed:11243866).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 296296Missing in isoform 4. 1 PublicationVSP_007897Add
BLAST
Alternative sequencei1 – 214214Missing in isoform 3. 2 PublicationsVSP_007896Add
BLAST
Alternative sequencei1 – 195195Missing in isoform 2. 2 PublicationsVSP_007895Add
BLAST
Alternative sequencei111 – 1144NVKI → ANGR in isoform 5. 1 PublicationVSP_007898
Alternative sequencei115 – 607493Missing in isoform 5. 1 PublicationVSP_007899Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050743 mRNA. Translation: BAB32653.1.
AB057758 mRNA. Translation: BAB41086.1.
AB057764 mRNA. Translation: BAB41092.1.
AB057765 mRNA. Translation: BAB41093.1.
AB057766 mRNA. Translation: BAB41094.1.
BC022608 mRNA. Translation: AAH22608.1.
BC106102 mRNA. Translation: AAI06103.1.
AK079850 mRNA. Translation: BAC37766.1.
CCDSiCCDS28372.2. [Q99N48-1]
CCDS28374.3. [Q99N48-2]
RefSeqiNP_113572.1. NM_031395.2. [Q99N48-1]
NP_899226.2. NM_183370.2. [Q99N48-2]
XP_006523321.1. XM_006523258.2. [Q99N48-1]
XP_006523322.1. XM_006523259.2. [Q99N48-1]
XP_006523324.1. XM_006523261.2. [Q99N48-2]
XP_006523326.1. XM_006523263.1. [Q99N48-2]
XP_006523327.1. XM_006523264.1. [Q99N48-2]
XP_006523328.1. XM_006523265.2. [Q99N48-4]
XP_011244483.1. XM_011246181.1. [Q99N48-1]
UniGeneiMm.442201.

Genome annotation databases

EnsembliENSMUST00000097430; ENSMUSP00000095041; ENSMUSG00000041831. [Q99N48-1]
ENSMUST00000160483; ENSMUSP00000123996; ENSMUSG00000041831. [Q99N48-2]
GeneIDi83672.
KEGGimmu:83672.
UCSCiuc008ahq.2. mouse. [Q99N48-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050743 mRNA. Translation: BAB32653.1.
AB057758 mRNA. Translation: BAB41086.1.
AB057764 mRNA. Translation: BAB41092.1.
AB057765 mRNA. Translation: BAB41093.1.
AB057766 mRNA. Translation: BAB41094.1.
BC022608 mRNA. Translation: AAH22608.1.
BC106102 mRNA. Translation: AAI06103.1.
AK079850 mRNA. Translation: BAC37766.1.
CCDSiCCDS28372.2. [Q99N48-1]
CCDS28374.3. [Q99N48-2]
RefSeqiNP_113572.1. NM_031395.2. [Q99N48-1]
NP_899226.2. NM_183370.2. [Q99N48-2]
XP_006523321.1. XM_006523258.2. [Q99N48-1]
XP_006523322.1. XM_006523259.2. [Q99N48-1]
XP_006523324.1. XM_006523261.2. [Q99N48-2]
XP_006523326.1. XM_006523263.1. [Q99N48-2]
XP_006523327.1. XM_006523264.1. [Q99N48-2]
XP_006523328.1. XM_006523265.2. [Q99N48-4]
XP_011244483.1. XM_011246181.1. [Q99N48-1]
UniGeneiMm.442201.

3D structure databases

ProteinModelPortaliQ99N48.
SMRiQ99N48. Positions 8-122, 266-596.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99N48. 2 interactions.
STRINGi10090.ENSMUSP00000095041.

PTM databases

iPTMnetiQ99N48.
PhosphoSiteiQ99N48.

Proteomic databases

EPDiQ99N48.
PaxDbiQ99N48.
PRIDEiQ99N48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000097430; ENSMUSP00000095041; ENSMUSG00000041831. [Q99N48-1]
ENSMUST00000160483; ENSMUSP00000123996; ENSMUSG00000041831. [Q99N48-2]
GeneIDi83672.
KEGGimmu:83672.
UCSCiuc008ahq.2. mouse. [Q99N48-1]

Organism-specific databases

CTDi94120.
MGIiMGI:1933367. Sytl3.

Phylogenomic databases

eggNOGiKOG1028. Eukaryota.
ENOG410XRME. LUCA.
GeneTreeiENSGT00810000125376.
HOVERGENiHBG103087.
InParanoidiQ99N48.
KOiK17598.
OMAiFVKGCLT.
OrthoDBiEOG7P02HG.
PhylomeDBiQ99N48.

Miscellaneous databases

PROiQ99N48.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N48.
CleanExiMM_SYTL3.
ExpressionAtlasiQ99N48. baseline and differential.
GenevisibleiQ99N48. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.30.40.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR010911. Rab_BD.
IPR028704. SYTL3.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR10024:SF222. PTHR10024:SF222. 1 hit.
PfamiPF00168. C2. 2 hits.
PF02318. FYVE_2. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50004. C2. 2 hits.
PS50916. RABBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type tandem C2 proteins."
    Fukuda M., Mikoshiba K.
    Biochem. Biophys. Res. Commun. 281:1226-1233(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH PHOSPHOLIPIDS; SUBCELLULAR LOCATION, INTERACTION WITH NRXN1.
    Strain: BALB/cJ.
    Tissue: Brain.
  2. "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3: identification of the Slp homology domain."
    Fukuda M., Saegusa C., Mikoshiba K.
    Biochem. Biophys. Res. Commun. 283:513-519(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY.
    Strain: BALB/cJ.
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary gland and Salivary gland.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. "The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical calcium-dependent phospholipid-binding machine: comparison with the C2A domain of synaptotagmin I."
    Fukuda M.
    Biochem. J. 366:681-687(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 336-GLU-GLU-337 AND 359-LYS--LYS-361, INTERACTION WITH PHOSPHOLIPIDS.
  6. "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain."
    Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.
    J. Biol. Chem. 277:9212-9218(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB27A.

Entry informationi

Entry nameiSYTL3_MOUSE
AccessioniPrimary (citable) accession number: Q99N48
Secondary accession number(s): Q3KQQ0
, Q8C506, Q99N47, Q99N49, Q99N54, Q99N79
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 25, 2003
Last modified: July 6, 2016
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.